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Xueting Wang Institute of Nautical Medicine, Nantong University, Nantong, Jiangsu, China
Co-innovation Center of Neuroregeneration, Nantong University, Nantong, Jiangsu, China

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Zhiran Zou Institute of Nautical Medicine, Nantong University, Nantong, Jiangsu, China
Co-innovation Center of Neuroregeneration, Nantong University, Nantong, Jiangsu, China

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Zhihui Yang Institute of Nautical Medicine, Nantong University, Nantong, Jiangsu, China
Co-innovation Center of Neuroregeneration, Nantong University, Nantong, Jiangsu, China

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Shan Jiang Institute of Nautical Medicine, Nantong University, Nantong, Jiangsu, China
Co-innovation Center of Neuroregeneration, Nantong University, Nantong, Jiangsu, China

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Yapeng Lu Institute of Nautical Medicine, Nantong University, Nantong, Jiangsu, China
Co-innovation Center of Neuroregeneration, Nantong University, Nantong, Jiangsu, China

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Dan Wang Institute of Nautical Medicine, Nantong University, Nantong, Jiangsu, China
Co-innovation Center of Neuroregeneration, Nantong University, Nantong, Jiangsu, China

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Zhangji Dong Co-innovation Center of Neuroregeneration, Nantong University, Nantong, Jiangsu, China
Key Laboratory of Neuroregeneration of Jiangsu and Ministry of Education, Nantong, Jiangsu, China

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Sha Xu Medical College of Soochow University, Suzhou, Jiangsu, China

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Li Zhu Institute of Nautical Medicine, Nantong University, Nantong, Jiangsu, China
Co-innovation Center of Neuroregeneration, Nantong University, Nantong, Jiangsu, China

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Introduction Hypoxia-inducible factor-1 (HIF1), a critical transcription factor, regulates cellular hypoxic response in oxygen-lacking cells and is rapidly degraded through the ubiquitin-proteasome pathway under normoxic conditions ( Semenza

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JME-18-0148
Volume/Issue:
Volume 62: Issue 1
Free access
Kenichi Kanai Laboratory of Molecular and Developmental Biology, Graduate School of Biological Science, Nara Institute of Science and Technology, 8916-5 Takayama-cho, Ikoma 630-0192, Japan

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Shinsaku Aramata Laboratory of Molecular and Developmental Biology, Graduate School of Biological Science, Nara Institute of Science and Technology, 8916-5 Takayama-cho, Ikoma 630-0192, Japan

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Sayo Katakami Laboratory of Molecular and Developmental Biology, Graduate School of Biological Science, Nara Institute of Science and Technology, 8916-5 Takayama-cho, Ikoma 630-0192, Japan

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Kunio Yasuda Laboratory of Molecular and Developmental Biology, Graduate School of Biological Science, Nara Institute of Science and Technology, 8916-5 Takayama-cho, Ikoma 630-0192, Japan

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Kohsuke Kataoka Laboratory of Molecular and Developmental Biology, Graduate School of Biological Science, Nara Institute of Science and Technology, 8916-5 Takayama-cho, Ikoma 630-0192, Japan

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Introduction MAFA is a member of the MAF family of basic leucine zipper transcription factors. In avians, MAFA/L-MAF has been identified as a neuroretina-specific transcript ( Benkhelifa et al . 1998 ) or a transcription factor that binds to the

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JME-11-0044
Volume/Issue:
Volume 47: Issue 1
Free access
M Hołysz Department of Biochemistry and Molecular Biology, Poznan University of Medical Sciences, 6 Swiecickiego St., 60-781 Poznan, Poland

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N Derebecka-Hołysz Department of Biochemistry and Molecular Biology, Poznan University of Medical Sciences, 6 Swiecickiego St., 60-781 Poznan, Poland

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W H Trzeciak Department of Biochemistry and Molecular Biology, Poznan University of Medical Sciences, 6 Swiecickiego St., 60-781 Poznan, Poland

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cholesteryl esters. All effects mentioned above are parts of the short-term regulation of steroidogenesis by ACTH and precede the long-term regulation involving stimulation of transcription of genes encoding steroidogenic cytochromes P450 ( CYP ), 3-β

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JME-10-0035
Volume/Issue:
Volume 46: Issue 1
Free access
Wiktoria Ratajczak Northern Ireland Centre for Stratified Medicine, School of Biomedical Sciences, Ulster University, C-TRIC Building, Altnagelvin Hospital Campus, Derry/Londonderry, Northern Ireland, UK

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Sarah D Atkinson Northern Ireland Centre for Stratified Medicine, School of Biomedical Sciences, Ulster University, C-TRIC Building, Altnagelvin Hospital Campus, Derry/Londonderry, Northern Ireland, UK

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Catriona Kelly Northern Ireland Centre for Stratified Medicine, School of Biomedical Sciences, Ulster University, C-TRIC Building, Altnagelvin Hospital Campus, Derry/Londonderry, Northern Ireland, UK

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-cell survival, glucose-stimulated insulin secretion and the expression of beta-cell markers and transcription factors regulating beta-cell maturation and function. Materials and methods Cell culture and treatment All initial experiments and

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JME-21-0076
Volume/Issue:
Volume 67: Issue 4
Restricted access
Chan Soo Shin Department of Internal Medicine, Seoul National University College of Medicine, 28 Yungun-Dong, Chongno-Gu, Seoul 110-744, Republic of Korea

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Min Jae Jeon Department of Internal Medicine, Seoul National University College of Medicine, 28 Yungun-Dong, Chongno-Gu, Seoul 110-744, Republic of Korea

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Jae-Yeon Yang Department of Internal Medicine, Seoul National University College of Medicine, 28 Yungun-Dong, Chongno-Gu, Seoul 110-744, Republic of Korea

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Sun-Ju Her Department of Internal Medicine, Seoul National University College of Medicine, 28 Yungun-Dong, Chongno-Gu, Seoul 110-744, Republic of Korea

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Dohee Kim Department of Internal Medicine, Seoul National University College of Medicine, 28 Yungun-Dong, Chongno-Gu, Seoul 110-744, Republic of Korea

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Sang Wan Kim Department of Internal Medicine, Seoul National University College of Medicine, 28 Yungun-Dong, Chongno-Gu, Seoul 110-744, Republic of Korea

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Seong Yeon Kim Department of Internal Medicine, Seoul National University College of Medicine, 28 Yungun-Dong, Chongno-Gu, Seoul 110-744, Republic of Korea

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Introduction The CCAAT/enhancer-binding proteins (C/EBPs) are members of the basic leucine zipper (bZIP) transcription factor family ( Landschulz et al. 1989 ), which are involved in the regulation of several biological processes

Article Type:
Research Article
DOI:
https://doi.org/10.1677/jme.1.01944
Volume/Issue:
Volume 36: Issue 3
Free access
Takanobu Sato Laboratory of Molecular Biology and Gene Regulation, Department of Life Science, School of Agriculture, Meiji University, 1-1-1 Higashi-mita, Tama-ku, Kawasaki, Kanagawa 214-8571, Japan

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Kousuke Kitahara Laboratory of Molecular Biology and Gene Regulation, Department of Life Science, School of Agriculture, Meiji University, 1-1-1 Higashi-mita, Tama-ku, Kawasaki, Kanagawa 214-8571, Japan

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Takao Susa Laboratory of Molecular Biology and Gene Regulation, Department of Life Science, School of Agriculture, Meiji University, 1-1-1 Higashi-mita, Tama-ku, Kawasaki, Kanagawa 214-8571, Japan

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Takako Kato Laboratory of Molecular Biology and Gene Regulation, Department of Life Science, School of Agriculture, Meiji University, 1-1-1 Higashi-mita, Tama-ku, Kawasaki, Kanagawa 214-8571, Japan

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Yukio Kato Laboratory of Molecular Biology and Gene Regulation, Department of Life Science, School of Agriculture, Meiji University, 1-1-1 Higashi-mita, Tama-ku, Kawasaki, Kanagawa 214-8571, Japan

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transcription factors were reported (for review, see Brown & McNeilly 1999 , Savage et al. 2003 , Jorgensen et al. 2004 ). We recently demonstrated that one of the DNA-binding proteins for the Fd2 region (−852/−746 bp) of the porcine FSH β gene

Article Type:
Research Article
DOI:
https://doi.org/10.1677/jme.1.02010
Volume/Issue:
Volume 37: Issue 2
Free access
Julie Amyot Montreal Diabetes Research Center, Department of Biochemistry, Division of Cellular and Molecular Biology, Medicine, Nutrition, Centre de Recherche du Centre Hospitalier de l'Université de Montréal (CRCHUM), Technopole Angus, 2901 Rachel Est, Montreal, Quebec H1W 4A4, Canada
Montreal Diabetes Research Center, Department of Biochemistry, Division of Cellular and Molecular Biology, Medicine, Nutrition, Centre de Recherche du Centre Hospitalier de l'Université de Montréal (CRCHUM), Technopole Angus, 2901 Rachel Est, Montreal, Quebec H1W 4A4, Canada

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Isma Benterki Montreal Diabetes Research Center, Department of Biochemistry, Division of Cellular and Molecular Biology, Medicine, Nutrition, Centre de Recherche du Centre Hospitalier de l'Université de Montréal (CRCHUM), Technopole Angus, 2901 Rachel Est, Montreal, Quebec H1W 4A4, Canada
Montreal Diabetes Research Center, Department of Biochemistry, Division of Cellular and Molecular Biology, Medicine, Nutrition, Centre de Recherche du Centre Hospitalier de l'Université de Montréal (CRCHUM), Technopole Angus, 2901 Rachel Est, Montreal, Quebec H1W 4A4, Canada

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Ghislaine Fontés Montreal Diabetes Research Center, Department of Biochemistry, Division of Cellular and Molecular Biology, Medicine, Nutrition, Centre de Recherche du Centre Hospitalier de l'Université de Montréal (CRCHUM), Technopole Angus, 2901 Rachel Est, Montreal, Quebec H1W 4A4, Canada

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Derek K Hagman Montreal Diabetes Research Center, Department of Biochemistry, Division of Cellular and Molecular Biology, Medicine, Nutrition, Centre de Recherche du Centre Hospitalier de l'Université de Montréal (CRCHUM), Technopole Angus, 2901 Rachel Est, Montreal, Quebec H1W 4A4, Canada

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Mourad Ferdaoussi Montreal Diabetes Research Center, Department of Biochemistry, Division of Cellular and Molecular Biology, Medicine, Nutrition, Centre de Recherche du Centre Hospitalier de l'Université de Montréal (CRCHUM), Technopole Angus, 2901 Rachel Est, Montreal, Quebec H1W 4A4, Canada

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Tracy Teodoro Montreal Diabetes Research Center, Department of Biochemistry, Division of Cellular and Molecular Biology, Medicine, Nutrition, Centre de Recherche du Centre Hospitalier de l'Université de Montréal (CRCHUM), Technopole Angus, 2901 Rachel Est, Montreal, Quebec H1W 4A4, Canada

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Allen Volchuk Montreal Diabetes Research Center, Department of Biochemistry, Division of Cellular and Molecular Biology, Medicine, Nutrition, Centre de Recherche du Centre Hospitalier de l'Université de Montréal (CRCHUM), Technopole Angus, 2901 Rachel Est, Montreal, Quebec H1W 4A4, Canada

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Érik Joly Montreal Diabetes Research Center, Department of Biochemistry, Division of Cellular and Molecular Biology, Medicine, Nutrition, Centre de Recherche du Centre Hospitalier de l'Université de Montréal (CRCHUM), Technopole Angus, 2901 Rachel Est, Montreal, Quebec H1W 4A4, Canada

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Vincent Poitout Montreal Diabetes Research Center, Department of Biochemistry, Division of Cellular and Molecular Biology, Medicine, Nutrition, Centre de Recherche du Centre Hospitalier de l'Université de Montréal (CRCHUM), Technopole Angus, 2901 Rachel Est, Montreal, Quebec H1W 4A4, Canada
Montreal Diabetes Research Center, Department of Biochemistry, Division of Cellular and Molecular Biology, Medicine, Nutrition, Centre de Recherche du Centre Hospitalier de l'Université de Montréal (CRCHUM), Technopole Angus, 2901 Rachel Est, Montreal, Quebec H1W 4A4, Canada
Montreal Diabetes Research Center, Department of Biochemistry, Division of Cellular and Molecular Biology, Medicine, Nutrition, Centre de Recherche du Centre Hospitalier de l'Université de Montréal (CRCHUM), Technopole Angus, 2901 Rachel Est, Montreal, Quebec H1W 4A4, Canada
Montreal Diabetes Research Center, Department of Biochemistry, Division of Cellular and Molecular Biology, Medicine, Nutrition, Centre de Recherche du Centre Hospitalier de l'Université de Montréal (CRCHUM), Technopole Angus, 2901 Rachel Est, Montreal, Quebec H1W 4A4, Canada

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protein-folding capacity of the ER and triggers the UPR ( Scheuner & Kaufman 2008 ) in an attempt to 1) attenuate global protein synthesis, 2) increase transcription of molecular chaperones and foldases, and 3) activate ER-associated protein degradation

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JME-11-0016
Volume/Issue:
Volume 47: Issue 3
Free access
C M Klinge Department of Biochemistry and Molecular Biology, Center for Genetics and Molecular Medicine, University of Louisville School of Medicine, Louisville, Kentucky 40292, USA

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S C Jernigan Department of Biochemistry and Molecular Biology, Center for Genetics and Molecular Medicine, University of Louisville School of Medicine, Louisville, Kentucky 40292, USA

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K A Mattingly Department of Biochemistry and Molecular Biology, Center for Genetics and Molecular Medicine, University of Louisville School of Medicine, Louisville, Kentucky 40292, USA

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K E Risinger Department of Biochemistry and Molecular Biology, Center for Genetics and Molecular Medicine, University of Louisville School of Medicine, Louisville, Kentucky 40292, USA

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J Zhang Department of Biochemistry and Molecular Biology, Center for Genetics and Molecular Medicine, University of Louisville School of Medicine, Louisville, Kentucky 40292, USA

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response element (ERE) and (2) ‘tethering’, in which ER interacts with another DNA-bound transcription factor, e.g. Sp1 ( Safe 2001 ) or AP-1 ( Webb et al. 1995 ), in a way that stabilizes the DNA binding of that transcription factor in the absence of

Article Type:
Research Article
DOI:
https://doi.org/10.1677/jme.1.01541
Volume/Issue:
Volume 33: Issue 2
Free access
Ying Wang Department of Pharmacology and Therapeutics, McGill University, 3655 Promenade Sir William Osler, Montréal, Quebec, Canada H3G 1Y6

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Vanessa Libasci Department of Pharmacology and Therapeutics, McGill University, 3655 Promenade Sir William Osler, Montréal, Quebec, Canada H3G 1Y6

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Daniel J Bernard Department of Pharmacology and Therapeutics, McGill University, 3655 Promenade Sir William Osler, Montréal, Quebec, Canada H3G 1Y6

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stimulating the transcription of the FSHβ ( Fshb ) subunit gene, which is the rate-limiting step in the synthesis of the mature dimeric hormone ( Attardi & Miklos 1990 , Weiss et al . 1995 ). The mechanisms through which activins regulate Fshb were elusive

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JME-09-0142
Volume/Issue:
Volume 44: Issue 6
Free access
Tetsuya Tagami Department of Endocrinology and Metabolism, Clinical Research Institute, Kyoto Medical Center, National Hospital Organization, 1-1 Mukaihata-cho, Fukakusa, Fushimi-ku, Kyoto 612-8555, Japan

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Hiroyuki Yamamoto Department of Endocrinology and Metabolism, Clinical Research Institute, Kyoto Medical Center, National Hospital Organization, 1-1 Mukaihata-cho, Fukakusa, Fushimi-ku, Kyoto 612-8555, Japan

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Kenji Moriyama Department of Endocrinology and Metabolism, Clinical Research Institute, Kyoto Medical Center, National Hospital Organization, 1-1 Mukaihata-cho, Fukakusa, Fushimi-ku, Kyoto 612-8555, Japan

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Kuniko Sawai Department of Endocrinology and Metabolism, Clinical Research Institute, Kyoto Medical Center, National Hospital Organization, 1-1 Mukaihata-cho, Fukakusa, Fushimi-ku, Kyoto 612-8555, Japan

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Takeshi Usui Department of Endocrinology and Metabolism, Clinical Research Institute, Kyoto Medical Center, National Hospital Organization, 1-1 Mukaihata-cho, Fukakusa, Fushimi-ku, Kyoto 612-8555, Japan

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Akira Shimatsu Department of Endocrinology and Metabolism, Clinical Research Institute, Kyoto Medical Center, National Hospital Organization, 1-1 Mukaihata-cho, Fukakusa, Fushimi-ku, Kyoto 612-8555, Japan

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Mitsuhide Naruse Department of Endocrinology and Metabolism, Clinical Research Institute, Kyoto Medical Center, National Hospital Organization, 1-1 Mukaihata-cho, Fukakusa, Fushimi-ku, Kyoto 612-8555, Japan

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Introduction A subgroup of the nuclear receptor superfamily that includes the receptors for thyroid hormone (TRs), retinoic acid (RARs), and vitamin D are known to form heterodimers with retinoid X receptors (RXR) to modulate the transcription of

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JME-08-0153
Volume/Issue:
Volume 42: Issue 5
Free access